ID L7JSI3_TRAHO Unreviewed; 825 AA.
AC L7JSI3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN ORFNames=THOM_3077 {ECO:0000313|EMBL:ELQ74011.1};
OS Trachipleistophora hominis (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pleistophoridae;
OC Trachipleistophora.
OX NCBI_TaxID=72359 {ECO:0000313|EMBL:ELQ74011.1, ECO:0000313|Proteomes:UP000011185};
RN [1] {ECO:0000313|EMBL:ELQ74011.1, ECO:0000313|Proteomes:UP000011185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23133373; DOI=10.1371/journal.ppat.1002979;
RA Heinz E., Williams T.A., Nakjang S., Noel C.J., Swan D.C., Goldberg A.V.,
RA Harris S.R., Weinmaier T., Markert S., Becher D., Bernhardt J., Dagan T.,
RA Hacker C., Lucocq J.M., Schweder T., Rattei T., Hall N., Hirt R.P.,
RA Embley T.M.;
RT "The genome of the obligate intracellular parasite Trachipleistophora
RT hominis: new insights into microsporidian genome dynamics and reductive
RT evolution.";
RL PLoS Pathog. 8:E1002979-E1002979(2012).
CC -!- FUNCTION: Component of the FACT complex, a general chromatin factor
CC that acts to reorganize nucleosomes. The FACT complex is involved in
CC multiple processes that require DNA as a template such as mRNA
CC elongation, DNA replication and DNA repair. During transcription
CC elongation the FACT complex acts as a histone chaperone that both
CC destabilizes and restores nucleosomal structure. It facilitates the
CC passage of RNA polymerase II and transcription by promoting the
CC dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC subsequently promotes the reestablishment of the nucleosome following
CC the passage of RNA polymerase II. {ECO:0000256|RuleBase:RU367052}.
CC -!- SUBUNIT: Component of the FACT complex.
CC {ECO:0000256|RuleBase:RU367052}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367052}.
CC Chromosome {ECO:0000256|RuleBase:RU367052}.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC {ECO:0000256|RuleBase:RU367052}.
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DR EMBL; JH994088; ELQ74011.1; -; Genomic_DNA.
DR AlphaFoldDB; L7JSI3; -.
DR STRING; 72359.L7JSI3; -.
DR VEuPathDB; MicrosporidiaDB:THOM_3077; -.
DR HOGENOM; CLU_004627_1_0_1; -.
DR InParanoid; L7JSI3; -.
DR OMA; AYSVMKN; -.
DR Proteomes; UP000011185; Unassembled WGS sequence.
DR GO; GO:0035101; C:FACT complex; IEA:UniProtKB-UniRule.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.150; -; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR Gene3D; 2.30.29.210; FACT complex subunit Spt16p/Cdc68p; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR029148; FACT-Spt16_Nlobe.
DR InterPro; IPR013953; FACT_Spt16.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR InterPro; IPR040258; Spt16.
DR PANTHER; PTHR13980; CDC68 RELATED; 1.
DR PANTHER; PTHR13980:SF15; FACT COMPLEX SUBUNIT SPT16; 1.
DR Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR Pfam; PF08512; Rttp106-like_middle; 1.
DR Pfam; PF08644; SPT16; 1.
DR SMART; SM01285; FACT-Spt16_Nlob; 1.
DR SMART; SM01287; Rtt106; 1.
DR SMART; SM01286; SPT16; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000313|EMBL:ELQ74011.1};
KW Cell division {ECO:0000313|EMBL:ELQ74011.1};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU367052};
KW DNA damage {ECO:0000256|RuleBase:RU367052};
KW DNA repair {ECO:0000256|RuleBase:RU367052};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU367052}; Nucleus {ECO:0000256|RuleBase:RU367052};
KW Reference proteome {ECO:0000313|Proteomes:UP000011185};
KW Transcription {ECO:0000256|RuleBase:RU367052};
KW Transcription regulation {ECO:0000256|RuleBase:RU367052}.
FT DOMAIN 6..160
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 399..522
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 628..716
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 750..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..811
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 825 AA; 96623 MW; EA3C40C161C1F668 CRC64;
MVDSQLNLSQ FVRRLTKIQE SISMPLLIVL GKKLEVEDFG PNSALFIYLL NYEFPETLLL
ITKDTCYAVT STKKKEILES MRCTKLKVYE RMKDGSRDDF LKKELLKITD SVLMSDRNNL
QGHFCSTFIN IFKVSDFEMG SLFVDKEEEE IEYVEGAAMF CTYLMEEAIK MVKKGEVCIE
SKLERHLDTP DKPFDLKLSQ IEFSYNPRIV RDQDAITISI GVRHQSYSAE IQRVLFYDAE
NLEVYRLRNE KLRNGNFENL KSIGLLQREG LRRNENGTFV MKTDYENYTI IDVVKCTDGK
FEVLTDDITW NDNDKKDFVP DDFVIIREKT NIEKKRLSRQ KALEKEIEIN EHQKELMDKL
NDEMVRYYSD METTEPAETA DKKFIAYEKE SQLPRKNKLV VDRRNFGVLI PINGYMVPFH
IEYVKNCSLN GNDLRINFRE GEIIKSITYR SKAANSLYNE IGDTRREYVE RRETSNVGEQ
GTLCEIKGRR HILGDVKIKT EVRTQKKSKA GNLELHENGF KFHDTVILFN NIEHLFYQQG
DAYILHFKLT VPIIFNGKKA YNVQFYKEVV ENMSIDIMKL HPSQKERLEE EQEKIRQEMI
KAEYDNFIKN VENNSNLRID RVSKDVYFEG VPYRQNVQIR PSSTCLVYLL EPPFLVVDFE
KMEVANFERV NYVSRSFDLT FIFKDKTFMT ITSIDSRSMD YLREFIDSRN ICFIQTAQNI
NWNNLLKTIK EDPFTFYNDG GWSALQPIRE DDDQEESSAS TLSSPSSVSE STMSETEGED
ESLEEDVVAE EDDEDIVDLN EIDSGYESEE DEDEPPNKKR RRSKI
//
